RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/10610126http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10610126http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10610126http://www.w3.org/2000/01/rdf-schema#comment"His-Asp phosphorelays are evolutionary-conserved powerful biological tactics for intracellular signal transduction. Such a phosphorelay is generally made up of "sensor histidine (His)-kinases", "response regulators", and "histidine-containing (HPt) phosphotransmitters". Results from recent intensive studies suggested that in the higher plant Arabidopsis thaliana, His-Asp phosphorelays may be widely used for propagating environmental stimuli, such as phytohormones (e.g., ethylene and cytokinin). In this study, we characterized, in vitro, the putative cytokinin-responsive CKI1 His-kinase, in terms of His-Asp phosphorelays. It was demonstrated for the first time that the receiver domain in this sensor exhibits a strong phosphohistidine phosphatase activity toward some Arabidopsis HPt phosphotransmitters (AHP1 and AHP2), suggesting the functional importance of the receiver domain for a resumed interaction of the sensor His-kinase with other His-Asp phosphorelay components."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.org/dc/terms/identifier"doi:10.1271/bbb.63.1627"xsd:string
http://purl.uniprot.org/citations/10610126http://purl.org/dc/terms/identifier"doi:10.1271/bbb.63.1627"xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Mizuno T."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Mizuno T."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Nakamura A."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Nakamura A."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Suzuki T."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Suzuki T."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Imamura A."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Imamura A."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Kakimoto T."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Kakimoto T."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Ueguchi C."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/author"Ueguchi C."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/name"Biosci. Biotechnol. Biochem."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/name"Biosci. Biotechnol. Biochem."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/pages"1627-1630"xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/pages"1627-1630"xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/title"Biochemical characterization of a putative cytokinin-responsive His-kinase, CKI1, from Arabidopsis thaliana."xsd:string
http://purl.uniprot.org/citations/10610126http://purl.uniprot.org/core/title"Biochemical characterization of a putative cytokinin-responsive His-kinase, CKI1, from Arabidopsis thaliana."xsd:string